X-ray diffraction
2.3Å resolution

Structural basis for the catalytic activity of aspartate aminotransferase K258H lacking its pyridoxal-5'-phosphate-binding lysine residue


Function and Biology Details

Reactions catalysed:
(1a) L-kynurenine + 2-oxoglutarate = 4-(2-aminophenyl)-2,4-dioxobutanoate + L-glutamate
L-aspartate + 2-oxoglutarate = oxaloacetate + L-glutamate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Aspartate aminotransferase, mitochondrial Chain: A
Molecule details ›
Chain: A
Length: 401 amino acids
Theoretical weight: 45 KDa
Source organism: Gallus gallus
Expression system: unidentified
  • Canonical: P00508 (Residues: 23-423; Coverage: 95%)
Gene name: GOT2
Sequence domains: Aminotransferase class I and II
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: C2221
Unit cell:
a: 69.8Å b: 91.3Å c: 127.8Å
α: 90° β: 90° γ: 90°
R R work R free
0.172 not available not available
Expression system: unidentified